5kbh: Difference between revisions
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<StructureSection load='5kbh' size='340' side='right'caption='[[5kbh]], [[Resolution|resolution]] 2.55Å' scene=''> | <StructureSection load='5kbh' size='340' side='right'caption='[[5kbh]], [[Resolution|resolution]] 2.55Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5kbh]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5kbh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_calcoaceticus Acinetobacter calcoaceticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KBH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KBH FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.55Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3CH:3-CHLOROPHENOL'>3CH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
< | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5kbh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kbh OCA], [https://pdbe.org/5kbh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kbh RCSB], [https://www.ebi.ac.uk/pdbsum/5kbh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kbh ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/MOPR_ACIGI MOPR_ACIGI] Involved in the regulation of the phenol degradation pathway. Activates phenol hydroxylase expression in the presence of phenol.<ref>PMID:9023219</ref> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Acinetobacter calcoaceticus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Anand | [[Category: Anand R]] | ||
[[Category: Panjikar | [[Category: Panjikar S]] | ||
[[Category: Ray | [[Category: Ray S]] | ||
Revision as of 13:44, 27 September 2023
CRYSTAL STRUCTURE OF THE AROMATIC SENSOR DOMAIN OF MOPR IN COMPLEX WITH 3-CHLORO-PHENOLCRYSTAL STRUCTURE OF THE AROMATIC SENSOR DOMAIN OF MOPR IN COMPLEX WITH 3-CHLORO-PHENOL
Structural highlights
FunctionMOPR_ACIGI Involved in the regulation of the phenol degradation pathway. Activates phenol hydroxylase expression in the presence of phenol.[1] Publication Abstract from PubMedPhenol and its derivatives are common pollutants that are present in industrial discharge and are major xenobiotics that lead to water pollution. To monitor as well as improve water quality, attempts have been made in the past to engineer bacterial in vivo biosensors. However, due to the paucity of structural information, there is insufficiency in gauging the factors that lead to high sensitivity and selectivity, thereby impeding development. Here, we present the crystal structure of the sensor domain of MopR (MopRAB) from Acinetobacter calcoaceticus in complex with phenol and its derivatives to a maximum resolution of 2.5 A. The structure reveals that the N-terminal residues 21-47 possess a unique fold, which are involved in stabilization of the biological dimer, and the central ligand binding domain belongs to the "nitric oxide signaling and golgi transport" fold, commonly present in eukaryotic proteins that bind long-chain fatty acids. In addition, MopRAB nests a zinc atom within a novel zinc binding motif, crucial for maintaining structural integrity. We propose that this motif is crucial for orchestrated motions associated with the formation of the effector binding pocket. Our studies reveal that residues W134 and H106 play an important role in ligand binding and are the key selectivity determinants. Furthermore, comparative analysis of MopR with XylR and DmpR sensor domains enabled the design of a MopR binding pocket that is competent in binding DmpR-specific ligands. Collectively, these findings pave way towards development of specific/broad based biosensors, which can act as useful tools for detection of this class of pollutants. Structural Basis of Selective Aromatic Pollutant Sensing by the Effector Binding Domain of MopR, an NtrC Family Transcriptional Regulator.,Ray S, Gunzburg MJ, Wilce M, Panjikar S, Anand R ACS Chem Biol. 2016 Jun 30. PMID:27362503[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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